Iron is the most versatile of all biochemically active metals, with variability encompassing its electronic configuration, number of unpaired electrons, type of ligands and iron-complexes stability. The versatility of iron properties is transposed to the proteins it can be associated to, especially relevant in the case of heme proteins. In this Review, the structural and functional properties of heme proteins are revisited, with particular focus on c-type cytochromes. The genome of Geobacter bacteria encodes for an unusually high number of assorted c-type cytochromes and, for this reason, they are used in this Review as a showcase of the cytochrome diversity. In the last decades, a vast portfolio of cytochromes has been revealed in these bacteria, with most of them defining new classes, ranging from monoheme to the recently identified polymeric assembly of multiheme cytochromes that forms micrometer-long electrically conductive filaments. These discoveries were on pace with the development of modern NMR equipment and advances in protein isotopic labeling methods, which are also revisited in this Review. Finally, following the description of the current state of the art of Geobacter cytochromes, examples on how the available structural and functional information was explored to structurally map protein–protein and protein–ligand interacting regions in redox complexes, and hence elucidate Geobacter's respiratory pathways, are presented.
- Bacterial electroconductive nanowires
- Cytochrome c
- Heme group
- Iron atom
- Structure–function relationship